Table of Contents
ISRN Spectroscopy
Volume 2014, Article ID 290824, 6 pages
http://dx.doi.org/10.1155/2014/290824
Research Article

Fluorescence Spectroscopy Study on the Interaction of Acetal Cleavable Anionic Surfactants and Bovine Serum Albumin

School of Chemistry and Chemical Engineering, Shanxi University, Taiyuan, Shanxi 030006, China

Received 23 November 2013; Accepted 8 January 2014; Published 17 February 2014

Academic Editors: G. D’Errico, M. Mączka, and Y. Ueno

Copyright © 2014 Xin Zhang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The interactions between bovine serum albumin (BSA) and two cleavable anionic surfactants, sodium 3-[(2-nonyl-1,3-dioxolan-4-yl)methoxy]propane-1-sulfonate (SNPS) and sodium 3,3′-(2-nonyl-1,3-dioxane-5,5-diyl)bis(methylene)bis(oxy)dipropane-1-sulfonate (SNDPS), have been studied by means of fluorescence spectroscopy and thermodynamic analysis. The fluorescence of BSA is quenched via a static quenching mechanism with the addition of the surfactants. The binding constants of the surfactants and proteins have been measured, with (SNPS) = M−1 and (SNDPS) = 7.08 × 104 M−1, respectively. The interaction between surfactants and BSA is mainly of hydrophobic nature, based on the number of binding sites, n[n(SNPS) = 1.57, n(SNDPS) = 1.47], and the thermodynamic relationship. These results suggest that SNPS and SNDPS could be effective protein denaturants for protein separation and analysis.